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Physicochemical Characterization of a Biomimetic, Elastin-Inspired Polypeptide with Enhanced Thermoresponsive Properties and Improved Cell Adhesion
[Image: see text] Genetic engineering allows fine-tuning and controlling protein properties, thus exploiting the new derivatives to obtain novel materials and systems with improved capacity to actively interact with biological systems. The elastin-like polypeptides are tunable recombinant biopolymer...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10647011/ https://www.ncbi.nlm.nih.gov/pubmed/37890135 http://dx.doi.org/10.1021/acs.biomac.3c00782 |
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author | Bandiera, Antonella Colomina - Alfaro, Laura Sist, Paola Gomez d’Ayala, Giovanna Zuppardi, Federica Cerruti, Pierfrancesco Catanzano, Ovidio Passamonti, Sabina Urbani, Ranieri |
author_facet | Bandiera, Antonella Colomina - Alfaro, Laura Sist, Paola Gomez d’Ayala, Giovanna Zuppardi, Federica Cerruti, Pierfrancesco Catanzano, Ovidio Passamonti, Sabina Urbani, Ranieri |
author_sort | Bandiera, Antonella |
collection | PubMed |
description | [Image: see text] Genetic engineering allows fine-tuning and controlling protein properties, thus exploiting the new derivatives to obtain novel materials and systems with improved capacity to actively interact with biological systems. The elastin-like polypeptides are tunable recombinant biopolymers that have proven to be ideal candidates for realizing bioactive interfaces that can interact with biological systems. They are characterized by a thermoresponsive behavior that is strictly related to their peculiar amino acid sequence. We describe here the rational design of a new biopolymer inspired by elastin and the comparison of its physicochemical properties with those of another already characterized member of the same protein class. To assess the cytocompatibility, the behavior of cells of different origins toward these components was evaluated. Our study shows that the biomimetic strategy adopted to design new elastin-based recombinant polypeptides represents a versatile and valuable tool for the development of protein-based materials with improved properties and advanced functionality. |
format | Online Article Text |
id | pubmed-10647011 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-106470112023-11-15 Physicochemical Characterization of a Biomimetic, Elastin-Inspired Polypeptide with Enhanced Thermoresponsive Properties and Improved Cell Adhesion Bandiera, Antonella Colomina - Alfaro, Laura Sist, Paola Gomez d’Ayala, Giovanna Zuppardi, Federica Cerruti, Pierfrancesco Catanzano, Ovidio Passamonti, Sabina Urbani, Ranieri Biomacromolecules [Image: see text] Genetic engineering allows fine-tuning and controlling protein properties, thus exploiting the new derivatives to obtain novel materials and systems with improved capacity to actively interact with biological systems. The elastin-like polypeptides are tunable recombinant biopolymers that have proven to be ideal candidates for realizing bioactive interfaces that can interact with biological systems. They are characterized by a thermoresponsive behavior that is strictly related to their peculiar amino acid sequence. We describe here the rational design of a new biopolymer inspired by elastin and the comparison of its physicochemical properties with those of another already characterized member of the same protein class. To assess the cytocompatibility, the behavior of cells of different origins toward these components was evaluated. Our study shows that the biomimetic strategy adopted to design new elastin-based recombinant polypeptides represents a versatile and valuable tool for the development of protein-based materials with improved properties and advanced functionality. American Chemical Society 2023-10-27 /pmc/articles/PMC10647011/ /pubmed/37890135 http://dx.doi.org/10.1021/acs.biomac.3c00782 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Bandiera, Antonella Colomina - Alfaro, Laura Sist, Paola Gomez d’Ayala, Giovanna Zuppardi, Federica Cerruti, Pierfrancesco Catanzano, Ovidio Passamonti, Sabina Urbani, Ranieri Physicochemical Characterization of a Biomimetic, Elastin-Inspired Polypeptide with Enhanced Thermoresponsive Properties and Improved Cell Adhesion |
title | Physicochemical
Characterization of a Biomimetic,
Elastin-Inspired Polypeptide with Enhanced Thermoresponsive Properties
and Improved Cell Adhesion |
title_full | Physicochemical
Characterization of a Biomimetic,
Elastin-Inspired Polypeptide with Enhanced Thermoresponsive Properties
and Improved Cell Adhesion |
title_fullStr | Physicochemical
Characterization of a Biomimetic,
Elastin-Inspired Polypeptide with Enhanced Thermoresponsive Properties
and Improved Cell Adhesion |
title_full_unstemmed | Physicochemical
Characterization of a Biomimetic,
Elastin-Inspired Polypeptide with Enhanced Thermoresponsive Properties
and Improved Cell Adhesion |
title_short | Physicochemical
Characterization of a Biomimetic,
Elastin-Inspired Polypeptide with Enhanced Thermoresponsive Properties
and Improved Cell Adhesion |
title_sort | physicochemical
characterization of a biomimetic,
elastin-inspired polypeptide with enhanced thermoresponsive properties
and improved cell adhesion |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10647011/ https://www.ncbi.nlm.nih.gov/pubmed/37890135 http://dx.doi.org/10.1021/acs.biomac.3c00782 |
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